Ion Mobility

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Herbert H. Hill - One of the best experts on this subject based on the ideXlab platform.

  • Ambient Pressure Inverse Ion Mobility Spectrometry Coupled to Mass Spectrometry.
    Analytical Chemistry, 2017
    Co-Authors: Austen L. Davis, William F. Siems, Brian H. Clowers, Herbert H. Hill
    Abstract:

    Although higher resolving powers are often achieved using ambient pressure drift tube Ion Mobility mass spectrometry (DT-IMMS) systems, lower duty cycles are often required which directly impacts sensitivity. Moreover, the mechanism of Ion gating using Bradbury-Nielsen or Tyndall-Gate configuratIons routinely results in Ion gate depletIon effects which discriminate against low Mobility Ions. This paper reports a new method of ambient pressure Ion Mobility operatIon in which inverse Ion Mobility spectrometry is coupled to a time-of-flight mass spectrometer to improve sensitivity and minimize the effects of Ion gate depletIon. In this mode of operatIon, the duty cycle is improved to approximate 99% from a typical value of less than 1%, improving the signal intensity by over 2 orders of magnitude. Another advantage of inverse Ion Mobility mass spectrometry is a reductIon of the impact of Ion gate depletIon on low Mobility molecules that translates into higher sensitivity for this class of analytes. To demons...

  • Ion Mobility spectrometer—field asymmetric Ion Mobility spectrometer-mass spectrometry
    International Journal for Ion Mobility Spectrometry, 2011
    Co-Authors: Matthew J. Pollard, Christopher K. Hilton, Kimberly Kaplan, Richard A. Yost, Herbert H. Hill
    Abstract:

    Since the development of electrospray IonizatIon (ESI) for Ion Mobility spectrometry mass spectrometry (IMMS), IMMS have been extensively applied for characterizatIon of gas-phase bio-molecules. ConventIonal Ion Mobility spectrometry (IMS), defined as drift tube IMS (DT-IMS), is typically a stacked ring design that utilizes a low electric field gradient. Field asymmetric Ion Mobility spectrometry (FAIMS) is a newer versIon of IMS, however, the geometry of the system is significantly different than DT-IMS and data are collected using a much higher electric field. Here we report constructIon of a novel ambient pressure dual gate DT-IMS coupled with a FAIMS system and then coupled to a quadrupole Ion trap mass spectrometer (QITMS) to form a hybrid three-dimensIonal separatIon instrument, DT-IMS-FAIMS-QITMS. The DT-IMS was operated at ~3 Townsend (electric field/number density (E/N) or (Td)) and was coupled in series with a FAIMS, operated at ~80 Td. Ions were Mobility-selected by the dual gate DT-IMS into the FAIMS and from the FAIMS the Ions were detected by the QITMS for as either MS or MSn. The system was evaluated using cocaine as an analytical standard and tested for the applicatIon of separating three isomeric tri-peptides: tyrosine-glycine-tryptophan (YGW), tryptophan-glycine-tyrosine (WGY) and tyrosine-tryptophan-glycine (YWG). All three tri-peptides were separated in the DT-IMS dimensIon and each had one Mobility peak. The samples were partially separated in the FAIMS dimensIon but two conformatIon peaks were detected for the YWG sample while YGW and WGY produced only one peak. Ion validatIon was achieved for all three samples using QITMS.

  • High-Pressure Ion Mobility Spectrometry
    Analytical chemistry, 2009
    Co-Authors: Eric J. Davis, Prabha Dwivedi, William F. Siems, Maggie Tam, Herbert H. Hill
    Abstract:

    The effects of above-ambient pressure on Ion Mobility on resolving power, resolutIon, and Ion current were investigated using a small, stand-alone Ion Mobility spectrometer (IMS). This work demonstrates the first example of Ion Mobility spectrometry at pressures above ambient. Ion Mobility spectra of chemical warfare agent (CWA) stimulant dimethyl methylphosphonate (DMMP) and several other standard compounds are shown for superambient conditIons. The IMS was operated at pressures from 700 to 4560 Torr. An optimal resolving power was obtained at a specific voltage as a functIon of pressure, with higher optimal resolving powers obtained at higher voltages, as predicted from standard IMS theory. At high pressures, however, resolving power did not increase as much as theory predicted, presumably due to Ion clustering. Nevertheless, an increase in pressure was found to improve resolutIon in IMS. One example where high pressure improved resolutIon was the separatIon of cyclohexylamine (K0 = 1.83) and 2-hexanone...

  • Ion Mobility-mass spectrometry.
    Journal of mass spectrometry : JMS, 2008
    Co-Authors: Abu B. Kanu, Prabha Dwivedi, Laura M Matz, Maggie Tam, Herbert H. Hill
    Abstract:

    This review article compares and contrasts various types of Ion Mobility-mass spectrometers available today and describes their advantages for applicatIon to a wide range of analytes. Ion Mobility spectrometry (IMS), when coupled with mass spectrometry, offers value-added data not possible from mass spectra alone. SeparatIon of isomers, isobars, and conformers; reductIon of chemical noise; and measurement of Ion size are possible with the additIon of Ion Mobility cells to mass spectrometers. In additIon, structurally similar Ions and Ions of the same charge state can be separated into families of Ions which appear along a unique mass-Mobility correlatIon line. This review describes the four methods of Ion Mobility separatIon currently used with mass spectrometry. They are (1) drift-time Ion Mobility spectrometry (DTIMS), (2) aspiratIon Ion Mobility spectrometry (AIMS), (3) differential-Mobility spectrometry (DMS) which is also called field-asymmetric waveform Ion Mobility spectrometry (FAIMS) and (4) traveling-wave Ion Mobility spectrometry (TWIMS). DTIMS provides the highest IMS resolving power and is the only IMS method which can directly measure collisIon cross-sectIons. AIMS is a low resolutIon Mobility separatIon method but can monitor Ions in a continuous manner. DMS and FAIMS offer continuous-Ion monitoring capability as well as orthogonal Ion Mobility separatIon in which high-separatIon selectivity can be achieved. TWIMS is a novel method of IMS with a low resolving power but has good sensitivity and is well intergrated into a commercial mass spectrometer. One hundred and sixty references on Ion Mobility-mass spectrometry (IMMS) are provided.

  • Ion Mobility mass spectrometry
    Journal of Mass Spectrometry, 2008
    Co-Authors: Abu B. Kanu, Prabha Dwivedi, Laura M Matz, Herbert H. Hill
    Abstract:

    This review article compares and contrasts various types of Ion Mobility–mass spectrometers available today and describes their advantages for applicatIon to a wide range of analytes. Ion Mobility spectrometry (IMS), when coupled with mass spectrometry, offers value-added data not possible from mass spectra alone. SeparatIon of isomers, isobars, and conformers; reductIon of chemical noise; and measurement of Ion size are possible with the additIon of Ion Mobility cells to mass spectrometers. In additIon, structurally similar Ions and Ions of the same charge state can be separated into families of Ions which appear along a unique mass-Mobility correlatIon line. This review describes the four methods of Ion Mobility separatIon currently used with mass spectrometry. They are (1) drift-time Ion Mobility spectrometry (DTIMS), (2) aspiratIon Ion Mobility spectrometry (AIMS), (3) differential-Mobility spectrometry (DMS) which is also called field-asymmetric waveform Ion Mobility spectrometry (FAIMS) and (4) traveling-wave Ion Mobility spectrometry (TWIMS). DTIMS provides the highest IMS resolving power and is the only IMS method which can directly measure collisIon cross-sectIons. AIMS is a low resolutIon Mobility separatIon method but can monitor Ions in a continuous manner. DMS and FAIMS offer continuous-Ion monitoring capability as well as orthogonal Ion Mobility separatIon in which high-separatIon selectivity can be achieved. TWIMS is a novel method of IMS with a low resolving power but has good sensitivity and is well intergrated into a commercial mass spectrometer. One hundred and sixty references on Ion Mobility–mass spectrometry (IMMS) are provided. Copyright © 2008 John Wiley & Sons, Ltd.

Brandon T Ruotolo - One of the best experts on this subject based on the ideXlab platform.

  • Ion Mobility-mass spectrometry for structural proteomics.
    Expert review of proteomics, 2012
    Co-Authors: Yueyang Zhong, Suk-joon Hyung, Brandon T Ruotolo
    Abstract:

    Ion Mobility coupled to mass spectrometry has been an important tool in the fields of chemical physics and analytical chemistry for decades, but its potential for interrogating the structure of proteins and multiprotein complexes has only recently begun to be realized. Today, Ion Mobility– mass spectrometry is often applied to the structural elucidatIon of protein assemblies that have failed high-throughput crystallizatIon or NMR spectroscopy screens. Here, we highlight the technology, approaches and data that have led to this dramatic shift in use, including emerging trends such as the integratIon of Ion Mobility–mass spectrometry data with more classical (e.g., ‘bottom-up’) proteomics approaches for the rapid structural characterizatIon of protein networks.

  • Ion Mobility–mass spectrometry analysis of large protein complexes
    Nature Protocols, 2008
    Co-Authors: Brandon T Ruotolo, Justin L P Benesch, Alan M Sandercock, Suk-joon Hyung, Carol V Robinson
    Abstract:

    Here we describe a detailed protocol for both data collectIon and interpretatIon with respect to Ion Mobility–mass spectrometry analysis of large protein assemblies. Ion Mobility is a technique that can separate gaseous Ions based on their size and shape. Specifically, within this protocol, we cover general approaches to data interpretatIon, methods of predicting whether specific model structures for a given protein assembly can be separated by Ion Mobility, and generalized strategies for data normalizatIon and modeling. The protocol also covers basic instrument settings and best practices for both observatIon and detectIon of large noncovalent protein complexes by Ion Mobility–mass spectrometry.

  • Ion Mobility mass spectrometry analysis of large protein complexes
    Nature Protocols, 2008
    Co-Authors: Brandon T Ruotolo, Justin L P Benesch, Alan M Sandercock, Suk-joon Hyung, Carol V Robinson
    Abstract:

    Here we describe a detailed protocol for both data collectIon and interpretatIon with respect to Ion Mobility–mass spectrometry analysis of large protein assemblies. Ion Mobility is a technique that can separate gaseous Ions based on their size and shape. Specifically, within this protocol, we cover general approaches to data interpretatIon, methods of predicting whether specific model structures for a given protein assembly can be separated by Ion Mobility, and generalized strategies for data normalizatIon and modeling. The protocol also covers basic instrument settings and best practices for both observatIon and detectIon of large noncovalent protein complexes by Ion Mobility–mass spectrometry.

  • ResolutIon equatIons for high-field Ion Mobility
    Journal of the American Society for Mass Spectrometry, 2004
    Co-Authors: Guido F. Verbeck, Brandon T Ruotolo, Kent J. Gillig, David H. Russell
    Abstract:

    An extensIon of current Mobility resolutIon equatIons as they apply to high-field Ion Mobility spectrometry is presented. The new resolutIon expressIon is applied to arrival time distributIons for Ions having a large range of Ion mobilities and mass-to-charge ratios (m/z). The results indicate that the new equatIon can be utilized to predict the Mobility resolutIon over a broader range of applied electric fields than previous Ion Mobility resolutIon expressIons.

J. I. Baumbach - One of the best experts on this subject based on the ideXlab platform.

Kevin Giles - One of the best experts on this subject based on the ideXlab platform.

  • Travelling wave Ion Mobility
    International Journal for Ion Mobility Spectrometry, 2013
    Co-Authors: Kevin Giles
    Abstract:

    The research papers in this issue of the InternatIonal Journal for Ion Mobility Spectrometry are the concluding articles of a two-part special issue on Travelling Wave Ion Mobility. The first issue, published in March (Volume 16, Issue 1, March 2013), covered a wide range of research areas: ‘Resolving the microcosmos of complex samples: UPLC/travelling wave Ion Mobility separatIon high resolutIon mass spectrometry for the analysis of in vivo drug metabolism studies’ by Blech and Laux; ‘The effects of catIon adductIon upon the conformatIon of three-helix bundle protein domains’ by Sokratous et al.; ‘Monitoring oligomer formatIon from self-aggregating amylin peptides using ESI-IMS-MS’ by Young et al.; ‘Traveling-wave Ion Mobility-mass spectrometry reveals additIonal mechanistic details in the stabilizatIon of protein complex Ions through tuned salt additives’ by Han and Ruotolo; 'Coupling electrospray corona discharge, charge reductIon and Ion Mobility mass spectrometry: From peptides to large macromolecular protein complexes' by Campuzano and Schnier; and 'Structural studies of metal ligand complexes by Ion Mobility-mass spectrometry' by Wright et al. The papers in this issue extend upon the range of studies presented in the first issue and together they illustrate the broad utility and applicability of (travelling wave) Ion Mobility—mass spectrometry. Since the launch of the first travelling wave Ion Mobility system (SYNAPT) some 7 years ago, the interest in Ion Mobility coupled with mass spectrometry has grown tremendously and shows no sign of abating. We continue to push the boundaries of Ion Mobility instrumentatIon design and, together with our customers and collaborators, work to extend the applicatIons of this technology. I am indebted to the small cross-sectIon of our customers/collaborators who have taken the time to contribute to this special issue on Travelling Wave Ion Mobility and offer my sincere thanks.

  • enhancements in travelling wave Ion Mobility resolutIon
    Rapid Communications in Mass Spectrometry, 2011
    Co-Authors: Kevin Giles, Jonathan P Williams, Iain Campuzano
    Abstract:

    The use of Ion Mobility separatIon to determine the collisIon cross-sectIon of a gas-phase Ion can provide valuable structural informatIon. The introductIon of travelling-wave Ion Mobility within a quadrupole/time-of-flight mass spectrometer has afforded routine collisIon cross-sectIon measurements to be performed on a range of Ionic species differing in gas-phase size/structure and molecular weight at physiologically relevant concentratIons. Herein we discuss the technical advances in the second-generatIon travelling-wave Ion Mobility separator, which result in up to a four-fold increase in Mobility resolutIon. This improvement is demonstrated using two reverse peptides (mw 490 Da), small ruthenium-containing anticancer drugs (mw 427 Da), a cisplatin-modified protein (mw 8776 Da) and the noncovalent tetradecameric chaperone complex GroEL (mw 802 kDa). What is also shown are that the collisIon cross-sectIons determined using the second-generatIon Mobility separator correlate well with the previous generatIon and theoretically derived values. Copyright © 2011 John Wiley & Sons, Ltd.

Carol V Robinson - One of the best experts on this subject based on the ideXlab platform.

  • Ion Mobility–mass spectrometry analysis of large protein complexes
    Nature Protocols, 2008
    Co-Authors: Brandon T Ruotolo, Justin L P Benesch, Alan M Sandercock, Suk-joon Hyung, Carol V Robinson
    Abstract:

    Here we describe a detailed protocol for both data collectIon and interpretatIon with respect to Ion Mobility–mass spectrometry analysis of large protein assemblies. Ion Mobility is a technique that can separate gaseous Ions based on their size and shape. Specifically, within this protocol, we cover general approaches to data interpretatIon, methods of predicting whether specific model structures for a given protein assembly can be separated by Ion Mobility, and generalized strategies for data normalizatIon and modeling. The protocol also covers basic instrument settings and best practices for both observatIon and detectIon of large noncovalent protein complexes by Ion Mobility–mass spectrometry.

  • Ion Mobility mass spectrometry analysis of large protein complexes
    Nature Protocols, 2008
    Co-Authors: Brandon T Ruotolo, Justin L P Benesch, Alan M Sandercock, Suk-joon Hyung, Carol V Robinson
    Abstract:

    Here we describe a detailed protocol for both data collectIon and interpretatIon with respect to Ion Mobility–mass spectrometry analysis of large protein assemblies. Ion Mobility is a technique that can separate gaseous Ions based on their size and shape. Specifically, within this protocol, we cover general approaches to data interpretatIon, methods of predicting whether specific model structures for a given protein assembly can be separated by Ion Mobility, and generalized strategies for data normalizatIon and modeling. The protocol also covers basic instrument settings and best practices for both observatIon and detectIon of large noncovalent protein complexes by Ion Mobility–mass spectrometry.

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